Dennis Winge, Ph.D. is a Professor of Medicine in the Division of Hematology and Hematologic Malignancies, Department of Internal Medicine at the University of Utah School of Medicine. He is also a Research Professor of Biochemistry in the Department of Biochemistry at the University of Utah. He is Director of the Biological Chemistry PhD graduate program at the University.
Research in the Winge laboratory is focused on cellular mitochondria. One major focus is the biogenesis of the mitochondrial electron transfer respiratory complexes II, III and IV within this organelle. Improper assembly of these complexes are evident in inherited and acquired diseases of patients with cardiomyopathy, hepatopathy, and neurological disorders. A key step in assembly of these complexes is the formation of their essential flavin, heme, and iron-sulfur centers, which are inserted by the involvement of assembly factor proteins. Much of the current knowledge on the biogenesis of theses respiratory complexes was elucidated in Saccharomyces cerevisiae, and many of the known assembly factors are conserved in humans. Dr. Winge and his team seek to identify new proteins that mediate the biogenesis of succinate dehydrogenase, cytochrome c reductase and cytochrome c oxidase complexes, and then elucidate their mechanism of action. They use a combination of in vitro biochemical, in vivo cellular assays and genetic analyses in these pursuits. Specifically, they study how flavin and three iron-sulfur centers are formed in succinate dehydrogenase, how the heme andiron-sulfur centers are formed in cytochrome c reductase and the pathway of copper and heme a center formation in cytochrome oxidase. In these studies, research focuses on known assembly factors, as well as seeking novel factors that mediate formation of the redox centers.
Dr. Winge received his Bachelor of Arts in Chemistry (Honors) at Concordia College in Morehead, Minnesota, after which he attended Duke University, earning first his M.S. and then his Ph.D. in Biochemistry. He completed two Postdoctoral Fellowships in Biochemistry, one at the University of Geneva in Geneva, Switzerland, and one at Duke University. He joined the faculty at the University of Utah in 1979. He currently serves on the Editorial Board for the Journal of Biological Chemistry, and received status as a Fellow of the American Association for the Advancement of Science in 2010. He has served as supervisor and/or mentor for nearly 80 high school, undergraduate, graduate and doctoral students, as well as served as a member on over 50 Ph.D./Doctorate Thesis Committees for the Departments of Biochemistry, CVMB, Biology, Chemistry, Human Genetics, Oncological Sciences and Pathology. Since 1979, Dr. Winge has published nearly 220 journal articles, reviews, books and book chapters.
Research Statement
Research in the Winge laboratory is focused on cellular mitochondria. One major focus is the biogenesis of the mitochondrial electron transfer respiratory complexes II, III and IV within this organelle. Improper assembly of these complexes are evident in inherited and acquired diseases of patients with cardiomyopathy, hepatopathy, and neurological disorders. A key step in assembly of these complexes is the formation of their essential flavin, heme, and iron-sulfur centers, which are inserted by the involvement of assembly factor proteins. Much of the current knowledge on the biogenesis of theses respiratory complexes was elucidated in Saccharomyces cerevisiae, and many of the known assembly factors are conserved in in humans. We seek to identify new proteins that mediate the biogenesis of succinate dehydrogenase, cytochrome c reductase and cytochrome c oxidase complexes and elucidate their mechanism of action. We use a combination of in vitro biochemical, in vivo cellular assays and genetic analyses in these pursuits. Specifically, we are studying how flavin and three iron-sulfur centers are formed in succinate dehydrogenase, how the heme andiron-sulfur centers are formed in cytochrome c reductase and the pathway ofcopper and heme a center formation in cytochrome oxidase. In these studies we are focused on known assembly factors as well as seeking novel factors that mediate formation of the redox centers.
